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CA distance fluctuations for 2503091538024026680

---  normal mode 17  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
MET 246 0.88 SER 96 -1.04 LEU 264
PHE 212 1.15 VAL 97 -1.00 ILE 254
ASN 210 1.55 PRO 98 -1.34 ARG 267
ASN 210 1.76 SER 99 -1.06 PRO 128
THR 211 1.27 GLN 100 -1.27 PRO 128
ASN 210 1.26 LYS 101 -1.30 PRO 128
SER 166 0.96 THR 102 -1.22 PRO 128
PRO 152 0.86 TYR 103 -0.99 PRO 98
PRO 152 1.09 GLN 104 -0.86 PRO 98
PRO 152 1.03 GLY 105 -0.97 PRO 98
PRO 152 1.05 SER 106 -0.79 PRO 98
PRO 152 1.34 TYR 107 -0.66 SER 96
PRO 152 1.44 GLY 108 -0.64 PRO 98
PRO 152 1.40 PHE 109 -0.70 PRO 98
GLN 165 1.15 ARG 110 -1.28 THR 155
GLN 165 1.27 LEU 111 -1.71 ARG 156
ALA 129 1.45 GLY 112 -1.62 TYR 220
ALA 129 1.57 PHE 113 -1.72 PRO 219
PRO 128 1.42 LEU 114 -1.46 PRO 219
GLU 221 1.10 VAL 122 -1.10 PRO 219
GLU 221 1.34 THR 123 -1.11 VAL 218
GLU 221 1.23 CYS 124 -1.19 VAL 157
GLU 221 1.08 THR 125 -1.07 VAL 157
PRO 142 0.93 TYR 126 -1.33 ASN 268
PRO 142 1.22 SER 127 -1.03 THR 102
THR 231 1.44 PRO 128 -1.30 LYS 101
PHE 113 1.57 ALA 129 -0.91 LYS 101
VAL 143 1.52 LEU 130 -0.81 GLN 100
VAL 143 1.64 ASN 131 -1.11 GLN 100
VAL 143 1.70 LYS 132 -0.75 GLU 285
PRO 142 1.52 MET 133 -1.04 SER 269
PRO 142 1.52 MET 133 -1.04 SER 269
GLU 221 1.23 PHE 134 -0.81 VAL 157
GLU 221 1.37 CYS 135 -0.99 VAL 218
GLU 221 1.56 GLN 136 -0.88 VAL 218
GLU 221 1.70 LEU 137 -1.05 ASP 186
GLU 221 1.85 ALA 138 -0.88 ASP 186
GLU 221 1.81 LYS 139 -0.93 VAL 218
GLU 221 1.47 THR 140 -1.17 VAL 218
MET 133 1.36 CYS 141 -1.61 VAL 218
MET 133 1.34 CYS 141 -1.59 VAL 218
LYS 132 1.64 PRO 142 -1.44 VAL 218
LYS 132 1.70 VAL 143 -1.53 GLY 154
ASN 131 1.62 GLN 144 -1.67 GLY 154
ASN 131 1.37 LEU 145 -1.67 ASP 259
ASN 131 1.09 TRP 146 -1.60 THR 155
ASN 131 0.87 VAL 147 -1.18 THR 155
PRO 152 1.13 ASP 148 -1.01 THR 155
ASP 228 1.30 SER 149 -0.82 PRO 222
GLY 199 1.41 THR 150 -0.76 SER 96
GLU 198 1.36 PRO 151 -0.51 SER 96
GLY 108 1.44 PRO 152 -0.55 GLU 221
SER 106 0.78 PRO 153 -1.60 THR 230
SER 106 0.44 GLY 154 -1.68 THR 231
ASN 210 0.47 THR 155 -1.60 TRP 146
ASN 210 0.52 ARG 156 -1.71 LEU 111
ASN 210 0.49 VAL 157 -1.44 PHE 113
GLN 100 0.73 ARG 158 -1.10 CYS 124
ASN 200 0.69 ALA 159 -0.95 TYR 126
GLU 221 0.76 MET 160 -0.66 TYR 126
GLU 221 0.91 ALA 161 -0.80 SER 185
GLU 221 0.87 ILE 162 -0.82 SER 185
GLU 221 0.91 TYR 163 -0.94 SER 185
LEU 111 1.18 LYS 164 -0.74 SER 185
GLY 112 1.27 GLN 165 -0.81 SER 185
LEU 111 1.09 SER 166 -0.72 SER 185
LEU 111 1.09 SER 166 -0.72 SER 185
GLY 112 1.00 GLN 167 -0.85 SER 185
ASN 247 1.28 HIS 168 -0.97 SER 185
MET 246 0.82 MET 169 -0.80 SER 185
MET 246 1.26 THR 170 -0.72 SER 185
GLY 245 1.56 GLU 171 -0.89 THR 211
GLU 221 0.77 VAL 172 -0.98 SER 185
GLU 221 0.98 VAL 173 -1.14 SER 185
GLU 221 1.05 ARG 174 -1.32 SER 185
GLU 221 1.18 ARG 175 -1.70 SER 185
GLU 221 1.13 CYS 176 -1.70 SER 185
GLU 221 1.09 PRO 177 -1.25 SER 185
GLU 221 1.08 HIS 178 -1.42 GLY 187
GLU 221 1.24 HIS 179 -1.47 GLY 187
GLU 221 1.35 GLU 180 -0.83 SER 185
GLU 221 1.25 ARG 181 -0.83 GLY 187
PRO 222 0.94 SER 185 -1.70 ARG 175
PRO 222 0.98 ASP 186 -1.67 CYS 238
PRO 222 0.94 GLY 187 -1.47 HIS 179
PRO 222 1.05 LEU 188 -1.18 HIS 179
PRO 222 1.25 ALA 189 -0.97 SER 261
GLU 221 1.14 PRO 190 -1.19 PHE 212
GLU 221 1.56 PRO 191 -1.03 PHE 212
GLU 221 1.20 GLN 192 -0.97 PHE 212
GLU 221 1.12 HIS 193 -0.89 SER 185
GLU 221 1.24 LEU 194 -1.11 SER 185
GLU 221 1.18 ILE 195 -0.89 GLY 262
PRO 222 1.26 ARG 196 -1.02 SER 261
PHE 270 1.29 VAL 197 -0.99 SER 261
PRO 222 1.45 GLU 198 -0.82 SER 261
THR 150 1.41 GLY 199 -0.63 HIS 179
PRO 151 1.06 ASN 200 -0.76 SER 261
PRO 222 1.09 LEU 201 -1.06 SER 261
LEU 188 1.05 ARG 202 -1.76 ILE 232
PRO 222 0.82 VAL 203 -1.61 SER 261
LEU 188 0.84 GLU 204 -1.64 GLY 262
GLU 221 0.59 TYR 205 -1.41 SER 261
GLN 100 0.58 LEU 206 -1.20 GLY 262
GLN 100 0.78 ASP 207 -0.93 SER 261
SER 99 1.12 ASP 208 -0.83 PRO 190
PRO 98 1.43 ARG 209 -1.05 PRO 190
SER 99 1.76 ASN 210 -1.00 PRO 191
SER 99 1.60 THR 211 -0.92 PRO 191
PRO 98 1.36 PHE 212 -1.19 PRO 190
GLN 100 0.88 ARG 213 -0.68 SER 185
GLN 100 0.73 HIS 214 -0.80 SER 261
GLN 100 0.72 SER 215 -1.01 GLY 262
PRO 222 0.68 VAL 216 -1.29 GLY 262
GLN 100 0.58 VAL 217 -1.26 PHE 113
GLN 100 0.44 VAL 218 -1.68 PHE 113
ASN 210 0.39 PRO 219 -1.72 PHE 113
ASN 200 0.42 TYR 220 -1.62 GLY 112
ALA 138 1.85 GLU 221 -0.69 VAL 225
GLU 198 1.45 PRO 222 -0.89 ASP 148
GLY 199 1.29 PRO 223 -1.12 THR 155
PRO 151 1.23 GLU 224 -0.95 PRO 153
PRO 151 1.16 VAL 225 -0.72 PRO 153
THR 150 1.09 GLY 226 -1.11 PRO 153
THR 150 1.00 SER 227 -1.28 GLY 154
SER 149 1.30 ASP 228 -1.47 PRO 219
ASN 131 0.99 CYS 229 -1.55 THR 155
ASN 131 1.34 THR 230 -1.60 PRO 153
PRO 128 1.44 THR 231 -1.68 GLY 154
PHE 270 1.50 ILE 232 -1.76 ARG 202
PHE 270 1.49 HIS 233 -1.21 SER 260
VAL 272 1.32 TYR 234 -1.14 SER 261
GLU 221 1.51 ASN 235 -0.95 GLY 262
GLU 221 1.49 TYR 236 -1.04 ASP 186
GLU 221 1.51 MET 237 -1.39 ASP 186
GLU 221 1.39 CYS 238 -1.67 ASP 186
GLU 221 1.39 CYS 238 -1.67 ASP 186
GLU 221 1.34 ASN 239 -1.33 ASP 186
GLU 221 1.21 SER 240 -1.17 ASP 186
GLU 221 1.12 SER 241 -1.20 ASP 186
GLU 221 1.13 CYS 242 -1.35 ASP 186
GLU 221 1.10 MET 243 -1.41 SER 185
GLU 171 1.30 GLY 244 -1.16 SER 185
GLU 171 1.56 GLY 245 -1.08 SER 185
THR 170 1.26 MET 246 -0.92 SER 185
HIS 168 1.28 ASN 247 -0.89 SER 185
GLU 171 1.03 ARG 248 -0.99 SER 185
GLU 221 0.99 ARG 249 -1.01 SER 185
GLU 221 1.05 PRO 250 -0.93 SER 185
GLU 221 1.10 ILE 251 -0.82 SER 185
TYR 234 1.12 LEU 252 -0.69 VAL 97
VAL 197 1.13 THR 253 -0.76 VAL 97
VAL 197 0.93 ILE 254 -1.00 VAL 97
VAL 197 0.93 ILE 254 -1.00 VAL 97
PRO 152 0.88 ILE 255 -1.17 TYR 126
PRO 152 0.65 THR 256 -1.08 TYR 126
PRO 152 0.66 THR 256 -1.08 TYR 126
PRO 152 0.60 LEU 257 -1.07 LEU 111
LYS 101 0.74 GLU 258 -1.35 LEU 145
LYS 101 0.59 ASP 259 -1.67 LEU 145
LYS 101 0.47 SER 260 -1.62 THR 231
LYS 101 0.47 SER 261 -1.63 GLU 204
LYS 101 0.58 GLY 262 -1.64 GLU 204
LYS 101 0.73 ASN 263 -1.25 GLU 204
LYS 101 0.87 LEU 264 -1.04 SER 96
PRO 153 0.60 LEU 265 -0.90 SER 96
PRO 152 0.90 GLY 266 -1.08 PRO 98
PRO 152 0.91 ARG 267 -1.34 PRO 98
PRO 152 0.96 ASN 268 -1.33 TYR 126
LYS 164 0.96 SER 269 -1.30 TYR 126
ILE 232 1.50 PHE 270 -0.96 GLN 100
HIS 233 1.34 GLU 271 -0.60 VAL 97
TYR 234 1.32 VAL 272 -0.55 SER 185
TYR 234 1.32 VAL 272 -0.55 SER 185
GLU 221 1.28 ARG 273 -0.79 ASP 186
GLU 221 1.39 VAL 274 -1.00 ASP 186
GLU 221 1.32 CYS 275 -0.94 ASP 186
GLU 221 1.30 ALA 276 -0.81 ASP 186
GLU 221 1.17 CYS 277 -0.78 VAL 218
GLU 221 1.17 CYS 277 -0.78 VAL 218
GLU 221 1.19 PRO 278 -0.83 VAL 218
GLU 221 1.06 GLY 279 -0.84 PRO 219
GLU 221 0.99 ARG 280 -0.74 PRO 219
GLU 221 1.03 ASP 281 -0.67 ASP 186
GLU 221 1.01 ARG 282 -0.74 SER 269
GLU 221 0.93 ARG 283 -0.67 LYS 101
GLU 221 0.88 THR 284 -0.64 ASP 186
GLU 221 0.90 GLU 285 -0.75 LYS 132
PRO 142 1.12 GLU 286 -0.59 GLN 100
THR 231 0.92 GLU 287 -0.52 GLN 100

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 8th, 2025.